UHRF1 Antibody - C-terminal region (ARP32596_P050)
- Known as:
- UHRF1 Antibody - C-terminal region (ARP32596_P050)
- Catalog number:
- arp32596_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- UHRF1 Antibody - C-terminal region (ARP32596_P050)
Related genes to: UHRF1 Antibody - C-terminal region (ARP32596_P050)
- Gene:
- UHRF1 NIH gene
- Name:
- ubiquitin like with PHD and ring finger domains 1
- Previous symbol:
- -
- Synonyms:
- ICBP90, Np95, FLJ21925, RNF106, TDRD22
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-03-15
- Date modifiied:
- 2017-03-17
Related products to: UHRF1 Antibody - C-terminal region (ARP32596_P050)
Related articles to: UHRF1 Antibody - C-terminal region (ARP32596_P050)
- Small cell lung cancer (SCLC) is an aggressive neuroendocrine (NE) carcinoma characterized by early metastasis and an immune-cold microenvironment. We show that UHRF1, a chromatin-associated effector of RB1/E2F signaling, promotes SCLC growth and metastasis across major molecular subtypes. Using human SCLC cell lines, orthotopic and intracardiac xenografts, and genetically engineered mouse models, we found that loss of UHRF1 reduces proliferation, invasion, tumor burden, and metastasis while reprogramming tumors away from NE states toward an inflamed transcriptional program. UHRF1-deficient tumors upregulate chemokines and exhibit increased infiltration of CD8 T cells and myeloid populations. Mechanistically, UHRF1 interacts with PRC2 to reinforce NE lineage programs and suppress inflammatory gene expression. UHRF1 loss derepresses DNA-methylation-silenced tumor antigens, including MAGE-A4, highlighting a potential vulnerability that could be leveraged therapeutically. Together, these findings connect RB1 loss with chromatin repression, lineage control, and immune exclusion, highlighting UHRF1-dependent repression as a therapeutic vulnerability in SCLC. - Source: PubMed
Publication date: 2026/03/24
Gu YijunDe La Torre Jamie-JeanFazeli YasaminValenzuela J MateoGuzman FrederickTinoco RobertoBenavente Claudia A - Senile osteoporosis (SOP) is an age-related skeletal disorder characterized by progressive bone mineral density loss and deteriorated bone microarchitecture, imposing significant burdens on aging populations. Impaired osteogenesis of mesenchymal stem cells (MSCs) is a critical feature of SOP, yet its intrinsic mechanisms remain incompletely understood. - Source: PubMed
Publication date: 2026/04/17
Pang PeizhuoChen JunhuaLi QiboSu ZepengLin JiajieZeng YipengZhang WeihaoXiao ZipengChen ZibinLiu ZiqianLin YangfengZheng GuanYu WenhuiXie Zhongyu - DNA methylation is a stable epigenetic modification essential for promoter silencing, retrotransposon silencing, genomic imprinting, and X-chromosome inactivation. Symmetrical DNA methylation at CpG dinucleotides is maintained after every round of cell division by the DNMT1-UHRF1 maintenance methyltransferase complex. Here we define a conserved rank order of DNA hexanucleotide sequences surrounding CpG sites that determines baseline DNA methylation levels in cells and the probability that DNA methylation is retained across cell divisions. This rank order is conserved in vertebrates and does not depend on TET enzymatic activity. CpG sites in hexanucleotide sequences less favored by DNMT1 are more susceptible to replication-dependent loss of DNA methylation over time; consequently, the methylation status of these motifs serves as a marker of cumulative cell divisions, biological age and cancer progression. Thus, the intrinsic vulnerability stemming from the sequence preference of the DNMT1-UHRF1 complex compromises the long-term stability of DNA methylation, especially at heterochromatic sites in proliferating cells, and contributes to the epigenetic dysregulation observed in cancer and aging. - Source: PubMed
Publication date: 2026/04/11
López-Moyado Isaac FHernández-Espinosa LotAngel J CarlosModat AurélieLleshi ErmiraCrawford RobertFaulkner Geoffrey JRao Anjana - Mammalian oocytes store proteins for embryonic development on abundant structures known as cytoplasmic lattices (CPLs); however, the mechanisms by which they achieve this are unclear, largely because the molecular composition of the lattices themselves is unknown. Here, we use cryo-electron microscopy and artificial intelligence-based modeling to elucidate the molecular architecture and protein composition of native CPLs from mouse oocytes. We find that CPLs are formed by at least 13 different proteins assembling into a megadalton-scale complex, including multiple copies of maternal effect factors such as PADI6 and the subcortical maternal complex (SCMC). We show that proteins essential for early embryonic development are in fact structural components of the CPLs, including the cytoskeletal proteins α- and β-tubulin, which are incorporated into CPLs as unpolymerized dimers; and an array of ubiquitination factors such as the epigenetic regulator and E3 ligase UHRF1, ubiquitin-conjugating E2 enzymes, and ubiquitin ligase substrate adaptors. This represents an elegant molecular mechanism by which oocytes stockpile vital proteins through direct incorporation into highly stable supramolecular assemblies. Our structures solve the decades-long mystery of the CPLs, thereby providing a structural framework for understanding how disrupting stored maternal factors leads to infertility and developmental defects. - Source: PubMed
Publication date: 2026/04/15
Kılıç Zeynep Ilgınvan Loenhout JoyceChaillet Martenvan Es Robert MAlcaraz Paula SobrevalsVos Harmjan RNoteborn Willem E MLeung Miguel Ricardo - - Source: PubMed
Publication date: 2026/04/14
Hu ZekaiSun QiXia WeiliangHe Zenglei